Crystallization and preliminary crystallographic analysis of the human calcineurin homologous protein CHP2 bound to the cytoplasmic region of the Na+/H+ exchanger NHE1.

Abstract

Calcineurin homologous protein (CHP) is a Ca2+-binding protein that directly interacts with and regulates the activity of all plasma-membrane Na+/H+-exchanger (NHE) family members. In contrast to the ubiquitous isoform CHP1, CHP2 is highly expressed in cancer cells. To understand the regulatory mechanism of NHE1 by CHP2, the complex CHP2-NHE1 (amino acids 503-545) has been crystallized by the sitting-drop vapour-diffusion method using PEG 3350 as precipitant. The crystals diffract to 2.7 A and belong to a tetragonal space group, with unit-cell parameters a = b = 49.96, c = 103.20 A.

• Authors: Youssef Ben Ammar, Soichi Takeda, Mitsuaki Sugawara, Masashi Miyano, Hidezo Mori, Shigeo Wakabayashi
• Journal: Acta crystallographica. Section F, Structural biology and crystallization communications (Acta Crystallogr Sect F Struct Biol Cryst Commun) Vol. 61 Issue Pt 10 Pg. 956-8 (Oct 01 2005) ISSN: 1744-3091 [Electronic] England
• PMID: 16511206 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• CHP1 protein, human
• Calcium-Binding Proteins
• Cation Transport Proteins
• Membrane Proteins
• Protein Isoforms
• SLC9A1 protein, human
• Sodium-Hydrogen Exchanger 1
• Sodium-Hydrogen Exchangers
• Polyethylene Glycols
• Calcineurin

Topics

• Calcineurin (chemistry)
• Calcium-Binding Proteins (chemistry)
• Cation Transport Proteins (chemistry)
• Cell Membrane (metabolism)
• Crystallization
• Crystallography, X-Ray
• Cytoplasm (metabolism)
• Diffusion
• Electrophoresis, Polyacrylamide Gel
• Escherichia coli (metabolism)
• Humans
• Membrane Proteins (chemistry)
• Polyethylene Glycols (chemistry)
• Protein Isoforms
• Protein Structure, Tertiary
• Sodium-Hydrogen Exchanger 1
• Sodium-Hydrogen Exchangers (chemistry)
• Temperature